TY - JOUR
T1 - Protecting your tail
T2 - Regulation of cadherin degradation by p120-catenin
AU - Kowalczyk, Andrew P.
AU - Reynolds, Albert B.
N1 - Funding Information:
The authors are grateful to the colleagues in their laboratories for helpful comments and suggestions. Work in the Kowalczyk laboratory was supported by grants from the NIH (R01AR048266 and R21AR050779) and from the American Heart Association. The Reynolds laboratory acknowledges support from NIH/NCI grants CA55724, CA83068 and P50-CA95103.
PY - 2004/10
Y1 - 2004/10
N2 - Work in various model systems has yielded conflicting views of how p120-catenin participates in adherens junction assembly and regulation. A series of recent studies indicate that a core function of p120-catenin in mammalian cells is to regulate cadherin turnover by modulating the entry of cadherins into degradative endocytic pathways. By this mechanism, cellular levels of p120-catenin perform a 'rheostat' or 'set point' function that controls steady-state cadherin levels. These studies parallel a growing interest in the regulation of cadherin levels at the cell surface by membrane trafficking pathways. Collectively, the findings suggest exciting new roles for p120-catenin at the interface between cadherins and membrane trafficking machinery, and imply novel mechanisms by which p120-catenin may regulate cell adhesion and migration in the context of development and cancer.
AB - Work in various model systems has yielded conflicting views of how p120-catenin participates in adherens junction assembly and regulation. A series of recent studies indicate that a core function of p120-catenin in mammalian cells is to regulate cadherin turnover by modulating the entry of cadherins into degradative endocytic pathways. By this mechanism, cellular levels of p120-catenin perform a 'rheostat' or 'set point' function that controls steady-state cadherin levels. These studies parallel a growing interest in the regulation of cadherin levels at the cell surface by membrane trafficking pathways. Collectively, the findings suggest exciting new roles for p120-catenin at the interface between cadherins and membrane trafficking machinery, and imply novel mechanisms by which p120-catenin may regulate cell adhesion and migration in the context of development and cancer.
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U2 - 10.1016/j.ceb.2004.07.001
DO - 10.1016/j.ceb.2004.07.001
M3 - Review article
C2 - 15363802
AN - SCOPUS:4444317116
VL - 16
SP - 522
EP - 527
JO - Current Opinion in Cell Biology
JF - Current Opinion in Cell Biology
SN - 0955-0674
IS - 5
ER -
